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A solute-binding protein for iron transport in Streptococcus iniae

BACKGROUND: Streptococcus iniae (S. iniae) is a major pathogen that causes considerable morbidity and mortality in cultured fish worldwide. The pathogen's ability to adapt to the host affects the extent of infection, hence understanding the mechanisms by which S. iniae overcomes physiological s...

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Autores principales: Zou, Lili, Wang, Jun, Huang, Baofeng, Xie, Mingquan, Li, Anxing
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3014919/
https://www.ncbi.nlm.nih.gov/pubmed/21122131
http://dx.doi.org/10.1186/1471-2180-10-309
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author Zou, Lili
Wang, Jun
Huang, Baofeng
Xie, Mingquan
Li, Anxing
author_facet Zou, Lili
Wang, Jun
Huang, Baofeng
Xie, Mingquan
Li, Anxing
author_sort Zou, Lili
collection PubMed
description BACKGROUND: Streptococcus iniae (S. iniae) is a major pathogen that causes considerable morbidity and mortality in cultured fish worldwide. The pathogen's ability to adapt to the host affects the extent of infection, hence understanding the mechanisms by which S. iniae overcomes physiological stresses during infection will help to identify potential virulence determinants of streptococcal infection. Grow S. iniae under iron-restricted conditions is one approach for identifying host-specific protein expression. Iron plays an important role in many biological processes but it has low solubility under physiological condition. Many microorganisms have been shown to be able to circumvent this nutritional limitation by forming direct contacts with iron-containing proteins through ATP-binding cassette (ABC) transporters. The ABC transporter superfamilies constitute many different systems that are widespread among living organisms with different functions, such as ligands translocation, mRNA translation, and DNA repair. RESULTS: An ABC transporter system, named as mtsABC (metal transport system) was cloned from S. iniae HD-1, and was found to be involved in heme utilization. mtsABC is cotranscribed by three downstream genes, i.e., mtsA, mtsB, and mtsC. In this study, we cloned the first gene of the mtsABC transporter system (mtsA), and purified the corresponding recombinant protein MtsA. The analysis indicated that MtsA is a putative lipoprotein which binds to heme that can serve as an iron source for the microorganism, and is expressed in vivo during Kunming mice infection by S. iniae HD-1. CONCLUSIONS: This is believed to be the first report on the cloning the ABC transporter lipoprotein from S. iniae genomic DNA. Together, our data suggested that MtsA is associated with heme, and is expressed in vivo during Kunming mice infection by S. iniae HD-1 which indicated that it can be a potential candidate for S. iniae subunit vaccine.
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spelling pubmed-30149192011-01-05 A solute-binding protein for iron transport in Streptococcus iniae Zou, Lili Wang, Jun Huang, Baofeng Xie, Mingquan Li, Anxing BMC Microbiol Research Article BACKGROUND: Streptococcus iniae (S. iniae) is a major pathogen that causes considerable morbidity and mortality in cultured fish worldwide. The pathogen's ability to adapt to the host affects the extent of infection, hence understanding the mechanisms by which S. iniae overcomes physiological stresses during infection will help to identify potential virulence determinants of streptococcal infection. Grow S. iniae under iron-restricted conditions is one approach for identifying host-specific protein expression. Iron plays an important role in many biological processes but it has low solubility under physiological condition. Many microorganisms have been shown to be able to circumvent this nutritional limitation by forming direct contacts with iron-containing proteins through ATP-binding cassette (ABC) transporters. The ABC transporter superfamilies constitute many different systems that are widespread among living organisms with different functions, such as ligands translocation, mRNA translation, and DNA repair. RESULTS: An ABC transporter system, named as mtsABC (metal transport system) was cloned from S. iniae HD-1, and was found to be involved in heme utilization. mtsABC is cotranscribed by three downstream genes, i.e., mtsA, mtsB, and mtsC. In this study, we cloned the first gene of the mtsABC transporter system (mtsA), and purified the corresponding recombinant protein MtsA. The analysis indicated that MtsA is a putative lipoprotein which binds to heme that can serve as an iron source for the microorganism, and is expressed in vivo during Kunming mice infection by S. iniae HD-1. CONCLUSIONS: This is believed to be the first report on the cloning the ABC transporter lipoprotein from S. iniae genomic DNA. Together, our data suggested that MtsA is associated with heme, and is expressed in vivo during Kunming mice infection by S. iniae HD-1 which indicated that it can be a potential candidate for S. iniae subunit vaccine. BioMed Central 2010-12-01 /pmc/articles/PMC3014919/ /pubmed/21122131 http://dx.doi.org/10.1186/1471-2180-10-309 Text en Copyright ©2010 Zou et al; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (<url>http://creativecommons.org/licenses/by/2.0</url>), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Zou, Lili
Wang, Jun
Huang, Baofeng
Xie, Mingquan
Li, Anxing
A solute-binding protein for iron transport in Streptococcus iniae
title A solute-binding protein for iron transport in Streptococcus iniae
title_full A solute-binding protein for iron transport in Streptococcus iniae
title_fullStr A solute-binding protein for iron transport in Streptococcus iniae
title_full_unstemmed A solute-binding protein for iron transport in Streptococcus iniae
title_short A solute-binding protein for iron transport in Streptococcus iniae
title_sort solute-binding protein for iron transport in streptococcus iniae
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3014919/
https://www.ncbi.nlm.nih.gov/pubmed/21122131
http://dx.doi.org/10.1186/1471-2180-10-309
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